RNPA_LIMF3
ID RNPA_LIMF3 Reviewed; 114 AA.
AC B2GEU6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227};
DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227};
GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; OrderedLocusNames=LAF_1842;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC RNA substrates such as 4.5S RNA. The protein component plays an
CC auxiliary but essential role in vivo by binding to the 5'-leader
CC sequence and broadening the substrate specificity of the ribozyme.
CC {ECO:0000255|HAMAP-Rule:MF_00227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00227};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; AP008937; BAG28178.1; -; Genomic_DNA.
DR RefSeq; WP_003682289.1; NC_010610.1.
DR AlphaFoldDB; B2GEU6; -.
DR SMR; B2GEU6; -.
DR EnsemblBacteria; BAG28178; BAG28178; LAF_1842.
DR GeneID; 61200854; -.
DR KEGG; lfe:LAF_1842; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_9_1_9; -.
DR OMA; PEQKHFR; -.
DR OrthoDB; 2014742at2; -.
DR Proteomes; UP000001697; Chromosome.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00227; RNase_P; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT CHAIN 1..114
FT /note="Ribonuclease P protein component"
FT /id="PRO_1000100370"
SQ SEQUENCE 114 AA; 13355 MW; A260D083CD75B26A CRC64;
MKKSYRIKKE SDFQRVFETH NSVANHKFVI YQMQKPNQPH FRVGISVGKK VGNAVQRGWV
KRRIRQTLLE VKPELKQDVD FLVIARKSAA DLSMKEIKKN LVHALTLAHL FEEK